Intermolecular Disulfide Bond in the Dimerization of S-periaxin Mediated by Cys88 and Cys139

Overview

Journal Acta Biochim Biophys Sin (Shanghai)

Specialties Biochemistry
Biophysics

Date 2016 Mar 5

PMID 26940996

Citations 1

Authors

Yan Yang

Yemei Ren

Yawei Shi

Affiliations

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Abstract

Periaxin is expressed in mammalian Schwann cells and lens fiber cells, and has been identified in a screen for cytoskeleton-associated proteins. Charcot-Marie-Tooth 4F is caused by losses or mutations of theperiaxingene. Theperiaxingene encodes two protein isoforms, namely, L-periaxin and S-periaxin.S-periaxin contains 147 amino acid residues and has an N-terminal PDZ domain. In this paper, S-periaxin was reported to be homodimerized through the formation of intermolecular disulfide bonds with its Cys88 and Cys139 residues under mild oxidation conditions. The covalent dimer of S-periaxin was also observed by western blot analysis and bimolecular fluorescence complementation analyses. S-periaxin dimerization formation could be regulated by cellular redox fluctuations. These results offer a possible mechanism to the formation of periaxin complexes, improvement of complex stability, and establishment of a link between the extracellular matrix and the cytoskeleton.

Citing Articles

Novel mutation in the periaxin gene causal to Charcot-Marie-Tooth disease type 4F.

Chen Y, Zhang H, Meng L, Tang X, Gong T, Yin J J Int Med Res. 2019; 48(2):300060519862064.

PMID: 31426691 PMC: 7581982. DOI: 10.1177/0300060519862064.

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